Direkt zum Inhalt
Merck
Alle Fotos(1)

Key Documents

MABN687

Sigma-Aldrich

Anti-β-amyloid fibril-specific, clone B10, AP Antibody

clone B10, from camel, alkaline phosphatase conjugate

Synonym(e):

Amyloid beta A4 protein, ABPP, APPI, APP, Alzheimer disease amyloid protein, Cerebral vascular amyloid peptide, CVAP, PreA4, Protease nexin-II, PN-II, N-APP2.Soluble APP-alpha, S-APP-alpha, Soluble APP-beta, S-APP-beta, C99, Beta-amyloid protein 42, Beta

Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise


About This Item

UNSPSC-Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

Biologische Quelle

camel

Qualitätsniveau

Konjugat

alkaline phosphatase conjugate

Antikörperform

purified immunoglobulin

Antikörper-Produkttyp

primary antibodies

Klon

B10, monoclonal

Speziesreaktivität

human

Methode(n)

ELISA: suitable
dot blot: suitable
immunofluorescence: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable

Isotyp

IgG

NCBI-Hinterlegungsnummer

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... APP(351)

Allgemeine Beschreibung

Amyloid fibrils are naturally occurring polypeptide scaffolds with considerable importance for human health and disease. A recombinant antibody domain fragment termed B10 specifically recognizes an amyloid-specific and conformationally defined epitope. The specificity and conformational specificity have been established by various methods, including, surface plasmon resonance, immunoblots, and immunohistochemistry. All these methods demonstrate that this antibody domain fragment distinguishes Aβ amyloid fibrils from disaggregated Aβ peptide as well as from specific Aβ oligomers. The antibody domain also possesses functional activity in preventing the formation of mature amyloid fibrils by stabilizing Aβ protofibrils, and recent data suggests that the B10 antibody fragment selectively binds to Alzheimer′s Aβ(1-40) amyloid fibrils and that fibril recognition depends on positively charged residues within the B10 antigen binding site. Mutation or alternation of specific residues changes B10’s interactions with various fibril configurations, implying that the B10 conformational specificity for amyloid fibrils depends upon specific electrostatic interactions with an acidic moiety, which is common to different amyloid fibrils.

Immunogen

Epitope: AB (1-40) amyloid fibrils

Anwendung

Anti-β-amyloid fibril-specific, clone B10, AP | MABN687 is an antibody against β-amyloid fibril-specific for use in Immunohistochemistry, Dot Blot, ELISA, Immunoprecipitation, Immunofluorescence.
This is a Camelid antibody fused to an alkaline phosphatase and does not require a secondary antibody for detection.
Dot Blot Analysis: A representative lot detected β-amyloid fibril-specific in synthetic Aβ (1–40) peptide (Habicht, G., et al. (2007). PNAS. 104(49):19232-19237).
Dot Blot Analysis: A representative lot detected β-amyloid fibril-specific in chemically modified fibrils (Haupt, C., et al. (2011). J. Mole. Biol. 405:341-348).
Elisa Analysis: A representative lot detected β-amyloid fibril-specific in N-biotinylated Aβ (1–40) conformers (disaggregated peptide, oligomers, or fibrils) (Morgado, I., et al. (2012). PNAS. 109(31):12503-12508).
Immunohistochemistry Analysis: A representative lot detected β-amyloid fibril-specific in Hippocampal sections from Alzheimer brain tissue (Habicht, G., et al. (2007). PNAS. 104(49):19232-19237).
Immunoprecipitation Analysis: A representative lot detected β-amyloid fibril-specific in native soluble and dispersible fractions from the brain lysates (Upadhaya, A.R., et al. (2014). BRAIN. 1-17).
Immunofluorescence Analysis: A representative lot detected β-amyloid fibril-specific in cell culture-derived amyloid plaques (Habicht, G., et al. (2007). PNAS. 104(49):19232-19237).

Qualität

Evaluated by Immunohistochemistry in human Alzheimer′s brain tissue.

Immunohistochemistry Analysis: A 1:50 dilution of this antibody detected β-amyloid fibril-specific in human Alzheimer′s brain tissue.

Physikalische Form

Ni-NTA agarose beads and Mono Q column
Purified Camelid monoclonal IgG in buffer containing 20mM NaH2PO4, 175mM NaCl, pH8.0 without preservatives.
Note: This is a Camelid antibody fused to an alkaline phosphatase and does not require a secondary antibody for detection.

Sonstige Hinweise

Concentration: Please refer to lot specific datasheet.

Sie haben nicht das passende Produkt gefunden?  

Probieren Sie unser Produkt-Auswahlhilfe. aus.

Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

nwg


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

Besitzen Sie dieses Produkt bereits?

In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Proceedings of the National Academy of Sciences of the United States of America
Habicht, G; Haupt, C; Friedrich, RP; Hortschansky, P; Sachse, C; Meinhardt, J; Wieligmann et al.
Proceedings of the National Academy of Sciences of the USA null
Christian Haupt et al.
Journal of molecular biology, 405(2), 341-348 (2010-11-10)
Amyloid fibrils are naturally occurring polypeptide scaffolds with considerable importance for human health and disease. These supermolecular assemblies are β-sheet rich and characterized by a high structural order. Clinical diagnosis and emerging therapeutic strategies of amyloid-dependent diseases, such as Alzheimer's
Proceedings of the National Academy of Sciences of the United States of America
Morgado, I; Wieligmann, K; Bereza, M; Ronicke, R; Meinhardt, K; Annamalai, K; Baumann et al.
Proceedings of the National Academy of Sciences of the USA null

Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..

Setzen Sie sich mit dem technischen Dienst in Verbindung.